[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 45-61. PubMed=2760073 [NCBI, ExPASy, EBI, Israel, Japan] Zhu X.-X., Kozarsky K., Strahler J.R., Eckerskorn C., Lottspeich F., Melhem R., Lowe J., Fox D.A., Hanash S.M., Atweh G.F.; "Molecular cloning of a novel human leukemia-associated gene. Evidence of conservation in animal species."; J. Biol. Chem. 264:14556-14560(1989).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0014-5793(90)80266-L; PubMed=2358074 [NCBI, ExPASy, EBI, Israel, Japan] Maucuer A., Doye V., Sobel A.; "A single amino acid difference distinguishes the human and the rat sequences of stathmin, a ubiquitous intracellular phosphoprotein associated with cell regulations."; FEBS Lett. 264:275-278(1990).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1917919 [NCBI, ExPASy, EBI, Israel, Japan] Melhem R.F., Zhu X., Hailat N., Strahler J.R., Hanash S.M.; "Characterization of the gene for a proliferation-related phosphoprotein (oncoprotein 18) expressed in high amounts in acute leukemia."; J. Biol. Chem. 266:17747-17753(1991).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8906359 [NCBI, ExPASy, EBI, Israel, Japan] Hosoya H., Ishikawa K., Dohi N., Marunouchi T.; "Transcriptional and post-transcriptional regulation of pr22 (Op18) with proliferation control."; Cell Struct. Funct. 21:237-243(1996).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan] Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; "The DNA sequence and biological annotation of human chromosome 1."; Nature 441:315-321(2006).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[7]	PROTEIN SEQUENCE OF 14-41 AND 44-52, AND MASS SPECTROMETRY. TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; Submitted (DEC-2008) to UniProtKB.
[8]	PROTEIN SEQUENCE OF 87-96. PubMed=2546936 [NCBI, ExPASy, EBI, Israel, Japan] Hanash S.M., Strahler J.R., Kuick R., Chu E.H.Y., Nichols D.; "Ca2+-dependent and cAMP-dependent control of nicotinic acetylcholine receptor phosphorylation in muscle cells."; J. Biol. Chem. 264:12813-12819(1989).
[9]	ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-25 AND SER-38, AND MASS SPECTROMETRY. PubMed=1737801 [NCBI, ExPASy, EBI, Israel, Japan] Labdon J.E., Nieves E., Schubart U.K.; "Analysis of phosphoprotein p19 by liquid chromatography/mass spectrometry. Identification of two proline-directed serine phosphorylation sites and a blocked amino terminus."; J. Biol. Chem. 267:3506-3513(1992).
[10]	PHOSPHORYLATION AT SER-25 AND SER-38. PubMed=8325880 [NCBI, ExPASy, EBI, Israel, Japan] Marklund U., Brattsand G., Shingler V., Gullberg M.; "Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase."; J. Biol. Chem. 268:15039-15047(1993).
[11]	PHOSPHORYLATION AT SER-16; SER-25 AND SER-38. PubMed=8245003 [NCBI, ExPASy, EBI, Israel, Japan] Marklund U., Brattsand G., Osterman O., Ohlsson P.-I., Gullberg M.; "Multiple signal transduction pathways induce phosphorylation of serines 16, 25, and 38 of oncoprotein 18 in T lymphocytes."; J. Biol. Chem. 268:25671-25680(1993).
[12]	PHOSPHORYLATION AT SER-16; SER-25 AND SER-38. DOI=10.1111/j.1432-1033.1994.tb18632.x; PubMed=8125092 [NCBI, ExPASy, EBI, Israel, Japan] Brattsand G., Marklund U., Nylander K., Roos G., Gullberg M.; "Cell-cycle-regulated phosphorylation of oncoprotein 18 on Ser16, Ser25 and Ser38."; Eur. J. Biochem. 220:359-368(1994).
[13]	INTERACTION WITH TUBULIN. DOI=10.1093/emboj/19.4.572; PubMed=10675326 [NCBI, ExPASy, EBI, Israel, Japan] Steinmetz M.O., Kammerer R.A., Jahnke W., Goldie K.N., Lustig A., van Oostrum J.; "Op18/stathmin caps a kinked protofilament-like tubulin tetramer."; EMBO J. 19:572-580(2000).
[14]	INTERACTION WITH TUBULIN. DOI=10.1074/jbc.275.10.6841; PubMed=10702243 [NCBI, ExPASy, EBI, Israel, Japan] Redeker V., Lachkar S., Siavoshian S., Charbaut E., Rossier J., Sobel A., Curmi P.A.; "Probing the native structure of stathmin and its interaction domains with tubulin. Combined use of limited proteolysis, size exclusion chromatography, and mass spectrometry."; J. Biol. Chem. 275:6841-6849(2000).
[15]	EFFECT OF PHOSPHORYLATION AT SER-63 ON TUBULIN BINDING. DOI=10.1093/embo-reports/kve105; PubMed=11415983 [NCBI, ExPASy, EBI, Israel, Japan] Steinmetz M.O., Jahnke W., Towbin H., Garcia-Echeverria C., Voshol H., Mueller D., van Oostrum J.; "Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin."; EMBO Rep. 2:505-510(2001).
[16]	TISSUE SPECIFICITY. DOI=10.1016/S0888-7543(03)00031-4; PubMed=12676564 [NCBI, ExPASy, EBI, Israel, Japan] Bieche I., Maucuer A., Laurendeau I., Lachkar S., Spano A.J., Frankfurter A., Levy P., Manceau V., Sobel A., Vidaud M., Curmi P.A.; "Expression of stathmin family genes in human tissues: non-neural-restricted expression for SCLIP."; Genomics 81:400-410(2003).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS SPECTROMETRY. DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan] Kim J.-E., Tannenbaum S.R., White F.M.; "Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; J. Proteome Res. 4:1339-1346(2005).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS SPECTROMETRY. TISSUE=T-cell; DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan] Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.; "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry."; Nat. Methods 2:591-598(2005).
[19]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 AND SER-63, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[20]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."; Nat. Biotechnol. 24:1285-1292(2006).
[21]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 AND SER-63, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan] Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; J. Proteome Res. 6:4150-4162(2007).
[22]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700120-MCP200; PubMed=17693683 [NCBI, ExPASy, EBI, Israel, Japan] Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."; Mol. Cell. Proteomics 6:1952-1967(2007).
[23]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-28; SER-38; SER-63 AND THR-146, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[24]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS SPECTROMETRY. DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan] Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Anal. Sci. 24:161-166(2008).
[25]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-25, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).
[26]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 AND SER-63, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

Comments

FUNCTION: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate fear (By similarity).
SUBUNIT: Binds to two alpha/beta-tubulin heterodimers. Interacts with KIST.
INTERACTION:
P46527:CDKN1B; NbExp=1; IntAct=EBI-445909, EBI-519280;
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Ubiquitous. Expression is strongest in fetal and adult brain, spinal cord, and cerebellum, followed by thymus, bone marrow, testis, and fetal liver. Expression is intermediate in colon, ovary, placenta, uterus, and trachea, and is readily detected at substantially lower levels in all other tissues examined. Lowest expression is found in adult liver.
PTM: Many different phosphorylated forms are observed depending on specific combinations among the sites which can be phosphorylated. MAPK is responsible for the phosphorylation of stathmin in response to NGF. Phosphorylation at Ser-16 seems to be required for neuron polarization (By similarity). Phosphorylation at Ser-63 reduces tubulin binding 10-fold and suppresses the MT polymerization inhibition activity.
DISEASE: Present in much greater abundance in cells from patients with acute leukemia of different subtypes than in normal peripheral blood lymphocytes, non-leukemic proliferating lymphoid cells, bone marrow cells, or cells from patients with chronic lymphoid or myeloid leukemia.
SIMILARITY: Belongs to the stathmin family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J04991; AAA59980.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M31303; AAA59971.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X53305; CAA37391.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z11566; CAA77660.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X94912; CAA64398.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL033528; CAC16020.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC082228; AAH82228.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00479997; -.

PIR

A40936; A40936.

RefSeq

NP_005554.1; -.
NP_981944.1; -.
NP_981946.1; -.

UniGene

Hs.209983

3D structure databases

DisProt

DP00174; -.

ModBase

P16949.

Protein-protein interaction databases

IntAct

P16949; 5.

PTM databases

PhosphoSite

P16949; -.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway; Aurora B signaling.
p38gammadeltapathway; Signaling mediated by p38-gamma and p38-delta.

2D gel databases

SWISS-2DPAGE

P16949; -.

DOSAC-COBS-2DPAGE

P16949; -.

REPRODUCTION-2DPAGE

IPI00479997; -.

Organism-specific databases

GC01M026099; -.

HIX0000281; -.

HGNC:6510; STMN1.

CAB010107; -.

151442; gene. [NCBI / EBI]

PharmGKB

PA35491; -.

Gene expression databases

P16949; -.

P16949; -.

HS_STMN1; -.

ENSG00000117632; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005874;	Cellular component: microtubule (inferred from electronic annotation from UniProtKB-KW).
GO:0004871;	Molecular function: signal transducer activity (traceable author statement from ProtInc).
GO:0015631;	Molecular function: tubulin binding (inferred from direct assay from MGI).
GO:0030154;	Biological process: cell differentiation (inferred from electronic annotation from UniProtKB-KW).
GO:0007242;	Biological process: intracellular signaling cascade (traceable author statement from ProtInc).
GO:0007019;	Biological process: microtubule depolymerization (inferred from direct assay from MGI).
GO:0007052;	Biological process: mitotic spindle organization (inferred from direct assay from MGI).
GO:0007399;	Biological process: nervous system development (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000956; Stathmin.
Graphical view of domain structure.

PANTHER

PTHR10104; Stathmin; 1.

Pfam

PF00836; Stathmin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF002285; Stathmin; 1.

PRINTS

PR00345; STATHMIN.

PROSITE

PS00563; STATHMIN_1; 1.
PS01041; STATHMIN_2; 1.

Proteomic databases

PeptideAtlas

P16949; -.

PRIDE

P16949; -.

Genome annotation databases

Ensembl

ENSG00000117632; Homo sapiens. [Contig view]

GeneID

3925; -.

KEGG

hsa:3925; -.

Phylogenomic databases

HOGENOM

P16949; -.

HOVERGEN

P16949; -.

OMA

P16949; KEAVPEF.

Other

15415; -.

STMN1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Coiled coil; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Microtubule; Neurogenesis; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 149`	`148`	`Stathmin.`	`PRO_0000182389`
`COILED`	`41 140`	`100`	`Potential.`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`MOD_RES`	`16 16`		`Phosphoserine.`
`MOD_RES`	`25 25`		`Phosphoserine; by CDC2 and MAPK.`
`MOD_RES`	`28 28`		`Phosphoserine.`
`MOD_RES`	`38 38`		`Phosphoserine; by CDC2.`
`MOD_RES`	`46 46`		`Phosphoserine (By similarity).`
`MOD_RES`	`63 63`		`Phosphoserine; by PKA.`
`MOD_RES`	`146 146`		`Phosphothreonine.`

Sequence information

Length: 149 AA [This is the length of the unprocessed precursor]

Molecular weight: 17303 Da [This is the MW of the unprocessed precursor]

CRC64: 316426F60DABCD01 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER 

        70         80         90        100        110        120 
RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL 

       130        140 
ERLREKDKHI EEVRKNKESK DPADETEAD

P16949 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools